Crystallization (Comment) | Organism |
---|---|
crystal structure | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
coproporphyrinogen-III + S-adenosyl-L-methionine | Escherichia coli | HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine | this enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine, AdoMet, instead of oxygen as oxidant, it occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase, the reaction starts by using an electron from the reduced form of the enzymes [4Fe-4S] cluster to split AdoMet into methionine and the radical 5-deoxyadenosin-5-yl, this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. The conversion of .CH-CH2-COO- leading to CH=CH2 + CO2 + e- replaces the electron initially used, reaction mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
coproporphyrinogen-III + S-adenosyl-L-methionine | HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis | Escherichia coli | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
? | |
coproporphyrinogen-III + S-adenosyl-L-methionine | HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine. The reaction involves the stereospecific hydrogen abstraction of the pro-S hydrogen from the propionate side chain beta-C of coproporphyrinogen-III, involvement of a coproporphyrinogenyl III radical, which is then decarboxylated releasing CO2 and forming the vinyl group, enzyme structure, two-domain enzyme consisting of the catalytic N- and an alpha-helical C-terminal domain, substrate binding mode | Escherichia coli | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
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Subunits | Comment | Organism |
---|---|---|
monomer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
Coprogen oxidase | - |
Escherichia coli |
coproporphyrinogen III oxidase | - |
Escherichia coli |
coproporphyrinogen oxidase | - |
Escherichia coli |
coproporphyrinogenase | - |
Escherichia coli |
HemN | - |
Escherichia coli |
More | member of the Radical SAM protein family | Escherichia coli |
oxidase, coproporphyrinogen | - |
Escherichia coli |
oxygen-independent coproporphyrinogen-III oxidase | - |
Escherichia coli |
radical SAM enzyme | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
4Fe-4S-center | structure, location and coordination of the cofactor, HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine | Escherichia coli |